Understand more about biomolecular characteristics, mechanisms and interactions

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Beyond α-helix and β-sheet - detect changes in secondary and tertiary structure

Today’s Chirascan circular dichroism spectrometers contribute to a deeper understanding of biomolecular characteristics, mechanisms and interactions by revealing far more about changes in higher order structure (HOS).

Analyzing proteins in solution reveals changes to their structural and thermodynamic properties. Application examples include:

  • Confirmation of structural integrity
  • Detection of minor changes in secondary and tertiary structure
  • Determining the effect of site-directed mutations on folding/unfolding (stability)
  • Monitoring response to changes in temperature or pH
  • Revealing the effect of denaturing agents or interaction partners.

Gain insight by detecting change

Gain insight and detect changes in secondary and tertiary structure

  • Detect minor differences under native or stressed conditions
  • Characterize protein stability
    • Determine response to thermal or chemical changes
    • Determine structural and thermodynamic properties
    • Study folding and unfolding mechanisms.

Secondary structure: far-UV
spectrum of a globular protein

Simultaneous acquisition of CD and absorbance spectra, 0.5 mm pathlength, Chirascan V100. Courtesy of leading research university, Germany

Tertiary structure: near-UV spectra
of two monoclonal antibodies

Differences between near-UV spectra due to slight changes in orientation of aromatic moieties, Chirascan V100, 10 mm pathlength

Further information

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